Tags

Type your tag names separated by a space and hit enter

Solution structure and functional characterization of jingzhaotoxin-XI: a novel gating modifier of both potassium and sodium channels.
Biochemistry. 2006 Dec 26; 45(51):15591-600.B

Abstract

JZTX-XI is a peptide toxin isolated from the venom of the Chinese spider Chilobrachys jingzhao. It contains 34 residues including six cysteine residues with disulfide bridges linked in the pattern of I-IV, II-V, and III-VI. Using 3'- and 5'-RACE methods, the full-length cDNA was identified as encoding an 86-residue precursor of JZTX-XI. In the electrophysiological assay, JZTX-XI shows activity toward the Kv2.1 channel in a way similar to hanatoxin1 and SGTx1 that both the activation and the deactivation processes are affected, which is in accordance with the high sequence homology among them (over 60% identity). On the other hand, JZTX-XI also exhibits specific interaction against the Nav channels of rat cardiac myocytes with a significant reduction in the peak current and slowing of channel inactivation. The solution structure of native JZTX-XI was determined by 1H NMR methods to identify the structural basis of these specific activities. Structural comparison of JZTX-XI with other gating modifier toxins shows that they all adopt a similar surface profile, a hydrophobic patch surrounded by charged residues such as Arg or Lys, which might be a common structural factor responsible for toxin-channel interaction. JZTX-XI might be an ideal tool to further investigate how spider toxins recognize various ion channels as their targets.

Authors+Show Affiliations

College of Life Sciences, Peking University, Beijing 100083, China.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17176080

Citation

Liao, Zhi, et al. "Solution Structure and Functional Characterization of jingzhaotoxin-XI: a Novel Gating Modifier of Both Potassium and Sodium Channels." Biochemistry, vol. 45, no. 51, 2006, pp. 15591-600.
Liao Z, Yuan C, Deng M, et al. Solution structure and functional characterization of jingzhaotoxin-XI: a novel gating modifier of both potassium and sodium channels. Biochemistry. 2006;45(51):15591-600.
Liao, Z., Yuan, C., Deng, M., Li, J., Chen, J., Yang, Y., Hu, W., & Liang, S. (2006). Solution structure and functional characterization of jingzhaotoxin-XI: a novel gating modifier of both potassium and sodium channels. Biochemistry, 45(51), 15591-600.
Liao Z, et al. Solution Structure and Functional Characterization of jingzhaotoxin-XI: a Novel Gating Modifier of Both Potassium and Sodium Channels. Biochemistry. 2006 Dec 26;45(51):15591-600. PubMed PMID: 17176080.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Solution structure and functional characterization of jingzhaotoxin-XI: a novel gating modifier of both potassium and sodium channels. AU - Liao,Zhi, AU - Yuan,Chunhua, AU - Deng,Meichun, AU - Li,Jiang, AU - Chen,Jinjun, AU - Yang,Yuejun, AU - Hu,Weijun, AU - Liang,Songping, PY - 2006/12/21/pubmed PY - 2008/1/12/medline PY - 2006/12/21/entrez SP - 15591 EP - 600 JF - Biochemistry JO - Biochemistry VL - 45 IS - 51 N2 - JZTX-XI is a peptide toxin isolated from the venom of the Chinese spider Chilobrachys jingzhao. It contains 34 residues including six cysteine residues with disulfide bridges linked in the pattern of I-IV, II-V, and III-VI. Using 3'- and 5'-RACE methods, the full-length cDNA was identified as encoding an 86-residue precursor of JZTX-XI. In the electrophysiological assay, JZTX-XI shows activity toward the Kv2.1 channel in a way similar to hanatoxin1 and SGTx1 that both the activation and the deactivation processes are affected, which is in accordance with the high sequence homology among them (over 60% identity). On the other hand, JZTX-XI also exhibits specific interaction against the Nav channels of rat cardiac myocytes with a significant reduction in the peak current and slowing of channel inactivation. The solution structure of native JZTX-XI was determined by 1H NMR methods to identify the structural basis of these specific activities. Structural comparison of JZTX-XI with other gating modifier toxins shows that they all adopt a similar surface profile, a hydrophobic patch surrounded by charged residues such as Arg or Lys, which might be a common structural factor responsible for toxin-channel interaction. JZTX-XI might be an ideal tool to further investigate how spider toxins recognize various ion channels as their targets. SN - 1520-4995 UR - https://www.unboundmedicine.com/medline/citation/17176080/Solution_structure_and_functional_characterization_of_jingzhaotoxin_XI:_a_novel_gating_modifier_of_both_potassium_and_sodium_channels_ L2 - https://doi.org/10.1021/bi061457+ DB - PRIME DP - Unbound Medicine ER -